Lysine 2,3-aminomutase

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Lysine 2,3-aminomutase (KAM or LAM) is a radical SAM enzyme that facilitates the conversion of the amino acid lysine to beta-lysine. It accomplishes this interconversion using three cofactors and a 5'-deoxyadenosyl radical formed in a S-Adenosyl methionine (SAM) activated radical reaction pathway.[1]

Structure

Shown on the right is the three-dimensional structure of the Lysine 2,3-aminomutase protein. The structure was determined by X-ray crystallography to 2.1 Angstrom resolution and was seen to crystallize as a homotetramer.[2] KAM was first purified and characterized in Clostridium subterminale for studies of Lysine metabolism.

Cofactors

Four key cofactors are required for the reaction catalyzed by the lysine 2,3-aminomutase enzyme. They are:

Reaction Mechanism

The generalized reaction takes place in 5 steps: The reaction mechanism described above is shown below:

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